scholarly journals Comprehensive Assessment of Nile Tilapia Skin (Oreochromis niloticus) Collagen Hydrogels for Wound Dressings

Marine Drugs ◽  
2020 ◽  
Vol 18 (4) ◽  
pp. 178 ◽  
Author(s):  
Baosheng Ge ◽  
Haonan Wang ◽  
Jie Li ◽  
Hengheng Liu ◽  
Yonghao Yin ◽  
...  
Keyword(s):  
Wound Dressing ◽  
Type I Collagen ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Wound Dressings ◽  
Type I ◽  
Rheological Characterization ◽  
Scanning Calorimetry ◽  
Soluble Collagen ◽  
Collagen Hydrogels

Collagen plays an important role in the formation of extracellular matrix (ECM) and development/migration of cells and tissues. Here we report the preparation of collagen and collagen hydrogel from the skin of tilapia and an evaluation of their potential as a wound dressing for the treatment of refractory wounds. The acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) were extracted and characterized using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), differential scanning calorimetry (DSC), circular dichroism (CD) and Fourier transform infrared spectroscopy (FTIR) analysis. Both ASC and PSC belong to type I collagen and have a complete triple helix structure, but PSC shows lower molecular weight and thermal stability, and has the inherent low antigenicity. Therefore, PSC was selected to prepare biomedical hydrogels using its self-aggregating properties. Rheological characterization showed that the mechanical strength of the hydrogels increased as the PSC content increased. Scanning electron microscope (SEM) analysis indicated that hydrogels could form a regular network structure at a suitable PSC content. Cytotoxicity experiments confirmed that hydrogels with different PSC content showed no significant toxicity to fibroblasts. Skin repair experiments and pathological analysis showed that the collagen hydrogels wound dressing could significantly accelerate the healing of deep second-degree burn wounds and the generation of new skin appendages, which can be used for treatment of various refractory wounds.

scholarly journals Preparation and Characterization of Thermally Stable Collagens from the Scales of Lizardfish (Synodus macrops)

Marine Drugs ◽  
2021 ◽  
Vol 19 (11) ◽  
pp. 597
Author(s):  
Junde Chen ◽  
Guangyu Wang ◽  
Yushuang Li
Keyword(s):  
Type I Collagen ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Type I ◽  
Salting Out ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Skin Collagen ◽  
Rat Tail

Marine collagen is gaining vast interest because of its high biocompatibility and lack of religious and social restrictions compared with collagen from terrestrial sources. In this study, lizardfish (Synodus macrops) scales were used to isolate acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC). Both ASC and PSC were identified as type I collagen with intact triple-helix structures by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and spectroscopy. The ASC and PSC had high amino acids of 237 residues/1000 residues and 236 residues/1000 residues, respectively. Thus, the maximum transition temperature (Tmax) of ASC (43.2 °C) was higher than that of PSC (42.5 °C). Interestingly, the Tmax of both ASC and PSC was higher than that of rat tail collagen (39.4 °C) and calf skin collagen (35.0 °C), the terrestrial collagen. Solubility tests showed that both ASC and PSC exhibited high solubility in the acidic pH ranges. ASC was less susceptible to the “salting out” effect compared with PSC. Both collagen types were nontoxic to HaCaT and MC3T3-E1 cells, and ASC was associated with a higher cell viability than PSC. These results indicated that ASC from lizardfish scales could be an alternative to terrestrial sources of collagen, with potential for biomedical applications.

scholarly journals Autophagy facilitates type I collagen synthesis in periodontal ligament cells

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Tomomi Nakamura ◽  
Motozo Yamashita ◽  
Kuniko Ikegami ◽  
Mio Suzuki ◽  
Manabu Yanagita ◽  
...  
Keyword(s):  
Periodontal Ligament ◽  
Collagen Synthesis ◽  
Type I Collagen ◽  
Periodontal Diseases ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Physiological Role ◽  
Type I ◽  
Periodontal Tissue ◽  
Pdl Cells

AbstractAutophagy is a lysosomal protein degradation system in which the cell self-digests its intracellular protein components and organelles. Defects in autophagy contribute to the pathogenesis of age-related chronic diseases, such as myocardial infarction and rheumatoid arthritis, through defects in the extracellular matrix (ECM). However, little is known about autophagy in periodontal diseases characterised by the breakdown of periodontal tissue. Tooth-supportive periodontal ligament (PDL) tissue contains PDL cells that produce various ECM proteins such as collagen to maintain homeostasis in periodontal tissue. In this study, we aimed to clarify the physiological role of autophagy in periodontal tissue. We found that autophagy regulated type I collagen synthesis by elimination of misfolded proteins in human PDL (HPDL) cells. Inhibition of autophagy by E-64d and pepstatin A (PSA) or siATG5 treatment suppressed collagen production in HPDL cells at mRNA and protein levels. Immunoelectron microscopy revealed collagen fragments in autolysosomes. Accumulation of misfolded collagen in HPDL cells was confirmed by sodium dodecyl sulfate–polyacrylamide gel electrophoresis. E-64d and PSA treatment suppressed and rapamycin treatment accelerated the hard tissue-forming ability of HPDL cells. Our findings suggest that autophagy is a crucial regulatory process that facilitates type I collagen synthesis and partly regulates osteoblastic differentiation of PDL cells.

Radioimmunoassay for the pyridinoline cross-linked carboxy-terminal telopeptide of type I collagen: a new serum marker of bone collagen degradation

1993 ◽  
Vol 39 (4) ◽  
pp. 635-640 ◽  
Author(s):  
J Risteli ◽  
I Elomaa ◽  
S Niemi ◽  
A Novamo ◽  
L Risteli
Keyword(s):  
Type I Collagen ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Bone Collagen ◽  
Collagen Molecule ◽  
Type I ◽  
Serum Samples ◽  
Amino Terminal ◽  
Wide Range ◽  
Carboxy Terminal

Abstract We developed a radioimmunoassay (RIA) for the carboxy-terminal telopeptides of type I collagen (ICTP), cross-linked with the helical domain of another type I collagen molecule, after isolation from human femoral bone. The cross-linked peptide was liberated by digesting insoluble, denatured bone collagen either with bacterial collagenase or with trypsin, and purified by two successive reversed-phase separations on HPLC, with monitoring of pyridinoline-specific fluorescence. The purity of the peptide was verified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and its origin in the type I collagen fibers was determined by amino-terminal amino acid sequencing. Polyclonal antibodies and a separation reagent containing second antibody and polyethylene glycol are used in the RIA. An immunologically identical, somewhat larger antigen is present in human serum; its concentration increases in multiple myeloma and in rheumatoid arthritis. The ICTP antigen seems to be cleared from the circulation by the kidneys, because glomerular filtration rates that are two-thirds of normal or less are associated with increased circulating ICTP concentrations. The CVs of the method are between 3% and 8% for a wide range of concentrations. The analysis of 40 serum samples can be completed in 4 h.

scholarly journals Comparison of the Structural Characteristics of Native Collagen Fibrils Derived from Bovine Tendons Using Two Different Methods: Modified Acid-Solubilized and Pepsin-Aided Extraction

Materials ◽  
2020 ◽  
Vol 13 (2) ◽  
pp. 358 ◽  
Author(s):  
Haiyan Ju ◽  
Xiuying Liu ◽  
Gang Zhang ◽  
Dezheng Liu ◽  
Yongsheng Yang
Keyword(s):  
Type I Collagen ◽  
Structural Characteristics ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Dry Weight ◽  
Collagen Fibrils ◽  
Type I ◽  
X Ray Diffraction ◽  
Aggregation Structure ◽  
Native Collagen

Native collagen fibrils (CF) were successfully extracted from bovine tendons using two different methods: modified acid-solubilized extraction for A-CF and pepsin-aided method for P-CF. The yields of A-CF and P-CF were up to 64.91% (±1.07% SD) and 56.78% (±1.22% SD) (dry weight basis), respectively. The analyses of both amino acid composition and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) confirmed that A-CF and P-CF were type I collagen fibrils. Both A-CF and P-CF retained the intact crystallinity and integrity of type I collagen’s natural structure by FTIR spectra, circular dichroism spectroscopy (CD) and X-ray diffraction detection. The aggregation structures of A-CF and P-CF were displayed by UV–Vis. However, A-CF showed more intact aggregation structure than P-CF. Microstructure and D-periodicities of A-CF and P-CF were observed (SEM and TEM). The diameters of A-CF and P-CF are about 386 and 282 nm, respectively. Although both A-CF and P-CF were theoretically concordant with the Schmitt hypothesis, A-CF was of evener thickness and higher integrity in terms of aggregation structure than P-CF. Modified acid-solubilized method provides a potential non-enzyme alternative to extract native collagen fibrils with uniform thickness and integral aggregation structure.

Radioimmunoassay of the carboxyterminal propeptide of human type I procollagen

1990 ◽  
Vol 36 (7) ◽  
pp. 1328-1332 ◽  
Author(s):  
J Melkko ◽  
S Niemi ◽  
L Risteli ◽  
J Risteli
Keyword(s):  
Type I Collagen ◽  
Soft Tissues ◽  
Polyacrylamide Gel Electrophoresis ◽  
Primary Cultures ◽  
Sodium Dodecyl ◽  
Type I ◽  
Lectin Affinity Chromatography ◽  
Human Type ◽  
Serum Antigen ◽  
Type I Procollagen

Abstract Type I collagen is the most abundant collagen type in soft tissues and the only type found in mineralized bone. We established a rapid equilibrium radioimmunoassay for the carboxyterminal propeptide of human type I procollagen (PICP), to be used as an indicator of the synthesis of type I collagen. We isolated type I procollagen from the medium of primary cultures of human skin fibroblasts, digested the protein with highly purified bacterial collagenase, and purified PICP by lectin-affinity chromatography, gel filtration, and ion-exchange separation on HPLC. The purity of the protein was verified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and by N-terminal amino acid sequencing of its component chains. The final radioimmunoassay was established with polyclonal rabbit antibodies. Material antigenically related to PICP is readily detected in human serum. There is only one form of the serum antigen, its molecular size and affinity to the antibodies being similar to those of the isolated propeptide. Intra- and interassay CVs are 3% and 5%, respectively. Preliminary reference intervals for healthy adults (18 to 61 years of age) are 38-202 micrograms/L for men and 50-170 micrograms/L for women: in men the concentration is inversely related to age. The serum antigen is stable during storage and after repeated thawing.

scholarly journals Polymeric C-terminal cross-linked material from type-I collagen. A modified method for purification, anomalous behaviour on gel filtration, molecular weight estimation, carbohydrate content and lipid content

1980 ◽  
Vol 189 (1) ◽  
pp. 111-124 ◽  
Author(s):  
N D Light ◽  
A J Bailey
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Type I Collagen ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Type I ◽  
Molecular Weight Range ◽  
Carbohydrate Analysis ◽  
Weight Range

Polymeric cross-linked C-terminal peptide material (poly-alpha 1CB6) from mature bovine tendon type-I collagen was prepared and purified by a modification of the method previously described [Light & Bailey (1980) Biochem. J. 185, 373-381]. Poly-alpha 1CB6 was shown to exhibit concentration-dependent aggregation effects on gel filtration due to interaction with a filtration medium. The material had an amino acid content that was very similar to a mixture of alpha 1CB6 and alpha 1CB5. The material was shown to be polydisperse with a mol.wt. range of 50 000-350 000, but chromatographic fractions were relatively homogeneous over this molecular weight range with respect to amino-acid composition. The heterogeneity of the material was not due to incomplete CNBr peptide cleavage, as poly-alpha 1CB6 did not contain detectable quantities of methionine. The material showed no discrete bands on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis but gave a constant blue stain throughout the molecular weight range described above. Lipid analysis showed that the partially purified material contained elevated levels of stearate when compared to the crude CNBr-digested starting material. This may indicate the specific association of a stearic-acid-rich lipid with the peptide material. On carbohydrate analysis poly-alpha 1CB6 was shown to contain only galactose and glucose at levels of 0.72 and 0.28% respectively. The carbohydrate and amino acid analyses indicated that (alpha 1CB6)2-(alpha 1CB5)1 may be the basic cross-linked structural unit of poly-alpha 1CB6)2-(alpha 1CB5)1 units, although the carbohydrate analysis indicated that the higher molecular weight oligomers may be enriched in alpha 1CB6.

scholarly journals Multi-scale mechanical characterization of highly swollen photo-activated collagen hydrogels

2015 ◽  
Vol 12 (102) ◽  
pp. 20141079 ◽  
Author(s):  
Giuseppe Tronci ◽  
Colin A. Grant ◽  
Neil H. Thomson ◽  
Stephen J. Russell ◽  
David J. Wood
Keyword(s):  
Mechanical Properties ◽  
Type I Collagen ◽  
Wound Care ◽  
Wound Dressings ◽  
Type I ◽  
Structure Property ◽  
Multi Scale ◽  
Macro Scale ◽  
Collagen Hydrogels ◽  
Tunable Mechanical Properties

Biological hydrogels have been increasingly sought after as wound dressings or scaffolds for regenerative medicine, owing to their inherent biofunctionality in biological environments. Especially in moist wound healing, the ideal material should absorb large amounts of wound exudate while remaining mechanically competent in situ . Despite their large hydration, however, current biological hydrogels still leave much to be desired in terms of mechanical properties in physiological conditions. To address this challenge, a multi-scale approach is presented for the synthetic design of cyto-compatible collagen hydrogels with tunable mechanical properties (from the nano- up to the macro-scale), uniquely high swelling ratios and retained (more than 70%) triple helical features. Type I collagen was covalently functionalized with three different monomers, i.e. 4-vinylbenzyl chloride, glycidyl methacrylate and methacrylic anhydride, respectively. Backbone rigidity, hydrogen-bonding capability and degree of functionalization ( F : 16 ± 12–91 ± 7 mol%) of introduced moieties governed the structure–property relationships in resulting collagen networks, so that the swelling ratio ( SR : 707 ± 51–1996 ± 182 wt%), bulk compressive modulus ( E c : 30 ± 7–168 ± 40 kPa) and atomic force microscopy elastic modulus ( E AFM : 16 ± 2–387 ± 66 kPa) were readily adjusted. Because of their remarkably high swelling and mechanical properties, these tunable collagen hydrogels may be further exploited for the design of advanced dressings for chronic wound care.

scholarly journals Human Adipose-Derived Stem Cell Secreted Extracellular Matrix Incorporated into Electrospun Poly(Lactic-co-Glycolic Acid) Nanofibrous Dressing for Enhancing Wound Healing

Polymers ◽  
2019 ◽  
Vol 11 (10) ◽  
pp. 1609 ◽  
Author(s):  
Tang ◽  
Yang ◽  
Lin ◽  
Chen ◽  
Lu ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Wound Healing ◽  
Growth Factors ◽  
Wound Dressing ◽  
Type I Collagen ◽  
Healing Process ◽  
Wound Dressings ◽  
Random Structure ◽  
Type I ◽  
Enhance Wound Healing

Wound dressing, which prevents dehydration and provides a physical barrier against infection to wound beds, can improve wound healing. The interactions between extracellular matrix (ECM) and growth factors is critical to the healing process. Electrospun nanofibers are promising templates for wound dressings due to the structure similarity to ECM of skin. Otherwise, the ECM secreted by human adipose-derived stem cells (hASCs) is rich in growth factors known to enhance wound healing. Accordingly, we propose that the PLGA nanofibrous template incorporated with hASCs-secreted ECM may enhance wound healing. In this study, PLGA nanofibrous matrixes with an aligned or a random structure were prepared by electrospinning. Human ASCs cultured on the aligned matrix had a better viability and produced a larger amount of ECM relative to that of random one. After 7 days’ cultivation, the hASCs on aligned PLGA substrates underwent decellularization to fabricate cECM/PLGA dressings. By using immunohistochemical staining against F-actin and cell nucleus, the removal of cellular components was verified. However, the type I collagen and laminin were well preserved on the cECM/PLGA nanofibrous matrixes. In addition, this substrate was hydrophilic, with appropriate mechanical strength to act as a wound dressing. The L929 fibroblasts had good activity, survival and proliferation on the cECM/PLGA meshes. In addition, the cECM/PLGA nanofibrous dressings improved the wound healing of surgically created full-thickness skin excision in a mouse model. This hASCs-secreted ECM incorporated into electrospun PLGA nanofibrous could be a promising dressing for enhancing wound healing.

scholarly journals Physicochemical and Functional Properties of Type I Collagens in Red Stingray (Dasyatis akajei) Skin

Marine Drugs ◽  
2019 ◽  
Vol 17 (10) ◽  
pp. 558 ◽  
Author(s):  
Junde Chen ◽  
Jianying Li ◽  
Zhongbao Li ◽  
Ruizao Yi ◽  
Shenjia Shi ◽  
...  
Keyword(s):  
Melting Temperature ◽  
Functional Properties ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Functional Materials ◽  
Type I ◽  
Liver Protein ◽  
Soluble Collagen ◽  
Red Stingray ◽  
Physicochemical And Functional Properties

Collagen is widely used in the pharmaceutical, tissue engineering, nutraceutical, and cosmetic industries. In this study, acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) were extracted from the skin of red stingray, and its physicochemical and functional properties were investigated. The yields of ASC and PSC were 33.95 ± 0.7% and 37.18 ± 0.71% (on a dry weight basis), respectively. ASC and PSC were identified as type I collagen by Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis (SDS-PAGE) analysis, possessing a complete triple helix structure as determined by UV absorption, Fourier transform infrared, circular dichroism, and X-ray diffraction spectroscopy. Contact angle experiments indicated that PSC was more hydrophobic than ASC. Thermal stability tests revealed that the melting temperature of PSC from red stingray skin was higher than that of PSC from duck skin, and the difference in the melting temperature between these two PSCs was 9.24 °C. Additionally, both ASC and PSC were functionally superior to some other proteins from terrestrial sources, such as scallop gonad protein, whey protein, and goose liver protein. These results suggest that PSC from red stingray skin could be used instead of terrestrial animal collagen in drugs, foods, cosmetics, and biological functional materials, and as scaffolds for bone regeneration.

scholarly journals Isolation and Comparative Study on the Characterization of Guanidine Hydrochloride Soluble Collagen and Pepsin Soluble Collagen from the Body of Surf Clam Shell (Coelomactra antiquata)

Foods ◽  
2019 ◽  
Vol 8 (1) ◽  
pp. 11 ◽  
Author(s):  
Jiulin Wu ◽  
Xiaoban Guo ◽  
Hui Liu ◽  
Li Chen
Keyword(s):  
Guanidine Hydrochloride ◽  
Polyacrylamide Gel Electrophoresis ◽  
Scientific Information ◽  
Sodium Dodecyl ◽  
The Body ◽  
Type I ◽  
Surf Clam ◽  
Clam Shell ◽  
Soluble Collagen ◽  
Pepsin Soluble Collagen

The aim of this study was to characterize the collagens from the body of surf clam shell (Coelomactra antiquata). Guanidine hydrochloride and pepsin were used to extract collagens. Guanidine hydrochloride soluble collagen (GSC) and pepsin soluble collagen (PSC) were separately isolated from the body of surf clam shell. Results showed that the moisture, protein, carbohydrate, and ash contents of the body of surf clam shell were 82.46%, 11.56%, 3.05%, and 2.38%, respectively, but the fat content was only 0.55%. The yields were 0.59% for GSC and 3.78% for PSC. Both GSC and PSC were composed of α1 and α2 chains and a β chain, however, GSC and PSC showed distinct differences from each other and the type I collagen from grass carp muscle on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). GSC and PSC contained glycine as the major amino acid and had imino acid of 150 and 155 residues/1000 residues, respectively. Fourier transform infrared spectroscopy (FTIR) spectra of GSC and PSC revealed the presence of a triple helix. The GSC appeared to have a dense sheet-like film linked by random-coiled filaments and PSC had fine globular filaments under scanning electron microscopy (SEM). The maximum transition temperature (Tmax) of GSC and PSC was 33.05 °C and 31.33 °C, respectively. These results provide valuable scientific information for the texture study and development of surf clam shell or other bivalve mollusks.

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